Our research focus

Most proteins are chemically modified in the cell and such modifications are often crucial for the protein’s ability to carry out its function. N-terminal acetylation is one of the most common protein modifications in eukaryotes. It is catalyzed by N-terminal acetyltransferases (NATs) which are linked to cancer, genetic syndromes, and regulation of human metabolism.

 

The focus of our lab is the molecular biology of protein N-terminal acetylation and NATs. We are using various eukaryotic model systems such as the budding yeast Saccharomyces cerevisiae, the nematode Caenorhabditis elegans, mammalian cell lines and zebrafish (Danio rerio), combined with in vitro approaches.

 

So far we and our collaborators have:

  • Elucidated the presumed complete cytosolic human NAT-machinery including the very first NAT enzyme acting post-translationally on a single dedicated substrate.

  • Quantitatively analysed the N-terminal acetylomes of yeast and human cells.

  • Developed novel assays for NAT-profiling.

  • Gained mechanistic insights of the cellular effects following NAT-knockdown.

  • Contributed to the understanding of the physiological and clinical importance of NATs by revealing the importance of NatA for cancer cell survival, the link between NatA and cancer cell drug sensitisation, and lately by identifying the first genetic disorders caused by NAT-mutations.

  • Solved the first structures of the NATs.

  • Developed the first potent NAT-inhibitors.

Last updated January 13, 2019.